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6C8Y

D30N HIV-1 protease in complex with a phenylboronic acid (P2') analog of darunavir

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 101
ChainResidue
ATHR74
AASN88
AHOH262
BARG141

site_idAC2
Number of Residues17
Detailsbinding site for residue BVR A 102
ChainResidue
AGLY49
AILE84
AHOH210
AHOH247
BASP125
BGLY127
BASP129
BASN130
BGLY148
BGLY149
BILE150
BVAL182
AASP25
AGLY27
AALA28
AASN30
AGLY48

site_idAC3
Number of Residues2
Detailsbinding site for residue CL B 201
ChainResidue
BTRP106
BLYS155

site_idAC4
Number of Residues3
Detailsbinding site for residue CL B 202
ChainResidue
BTHR174
BASN188
BHOH342

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL B 203
ChainResidue
AGLN18
AMET36
ASER37
BTHR112
BGLU165
BALA167
BGLY168
BHOH337

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADNTVI
ChainResidueDetails
AALA22-ILE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
ChainResidueDetails
AASP25
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE199

218853

PDB entries from 2024-04-24

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